Ursolic acid acetate and iso-mukaadial acetate bind to Plasmodium falciparum Hsp90, abrogating its chaperone function in vitro

Plasmodium falciparum is the most lethal malaria parasite. Increasing incidences of drug resistance of P. falciparum have prompted the need for discovering new and effective antimalarial compounds with an alternative mode of action. Heat shock protein 90 (PfHsp90) facilitates protein folding and is...

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Veröffentlicht in:	Naunyn-Schmiedeberg's archives of pharmacology 2024-07, Vol.397 (7), p.5179-5192
Hauptverfasser:	Nndwammbi, Andani A. T, Dongola, Tendamudzimu Harmfree, Shonhai, Addmore, Mokoena, Fortunate, Pooe, Ofentse J., Simelane, Mthokozisi B. C
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetates - chemistry Acetates - pharmacology Acetic acid Antimalarial activity Antimalarial agents Antimalarials - pharmacology Antiparasitic agents Antiprotozoal agents Biomedical and Life Sciences Biomedicine Citrate synthase Drug resistance Fourier transforms Heat shock proteins HSP90 Heat-Shock Proteins - metabolism Hsp90 protein Malaria Malate dehydrogenase Molecular Docking Simulation Molecular dynamics Molecular Dynamics Simulation Neurosciences Pharmacology/Toxicology Plasmodium falciparum Plasmodium falciparum - drug effects Protein Binding Protein folding Protein structure Protozoan Proteins - metabolism Secondary structure Surface Plasmon Resonance Therapeutic targets Triterpenes - chemistry Triterpenes - pharmacology Ursolic Acid
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